496-93-5 Usage
Description
L-Canaline, an aminooxy analog of ornithine, is a naturally occurring compound found in plants, particularly legumes. It is known for its ability to irreversibly inhibit aminotransferases (transaminases), such as ornithine aminotransferase, with a Ki value of 2 μM. L-Canaline forms oximes with α-keto acids and aldehydes, most notably with pyridoxal phosphate, which is an essential cofactor of aminotransferases. L-CANALINE BASE plays a role in the metabolism of L-canavanine, another aminooxy analog of arginine, and exhibits cytotoxic properties against various organisms, including bacteria, insects, and parasites.
Uses
Used in Pharmaceutical Industry:
L-Canaline is used as a pharmaceutical agent for its cytotoxic properties, targeting a range of organisms such as bacteria, insects, and parasites. Its ability to inhibit aminotransferases makes it a potential candidate for the development of new drugs to combat various diseases and infections.
Used in Metabolic Research:
L-Canaline is used as a research tool in the study of amino acid metabolism, particularly in the metabolism of L-canavanine, an aminooxy analog of arginine. Understanding the interactions between L-canavanine and L-canaline can provide insights into the regulation of amino acid metabolism and the development of novel therapeutic strategies.
Used in Plant Biology:
L-Canaline is used in plant biology to study the role of this compound in the natural defense mechanisms of plants, especially legumes. Its cytotoxic properties can help researchers understand how plants protect themselves against pests and pathogens, potentially leading to the development of more effective and environmentally friendly pest control methods.
Used in Biochemical Studies:
L-Canaline is used in biochemical research to investigate the formation of oximes with α-keto acids and aldehydes, particularly with pyridoxal phosphate. This research can contribute to a better understanding of the role of pyridoxal phosphate in aminotransferase activity and the potential development of new inhibitors or activators of these enzymes.
Synthesis Reference(s)
Tetrahedron, 23, p. 4441, 1967 DOI: 10.1016/S0040-4020(01)88842-6
in vitro
canaline strongly inhibited the activity of pyridoxal-dependent enzymes, including amino acid decarboxylases, 5-hydroxytryptophan decarboxylase, aminotransferases, tyrosine aminotransferase, ornithine transcarbamylase and plasma diamino-oxidase. the canaline inhibition was due to complex formation between canaline and the pyridoxal coenzyme. l-canaline is one of the most potent inhibitors of pyridoxal enzymes. the ic50 value of l-canaline against ornithine aminotransferase was 3 ×10-6m [4].
in vivo
intraperitoneal administration of 500 mg of dl-canaline/kg body wt. only produced a transient inhibition of oat in brain and liver by 65-70%, suggesting that dl-canaline was not a useful tool in studies of biological consequences of oat inhibition. [1].
references
[1] bolkenius f n, kndgen b, seiler n. dl-canaline and 5-fluoromethylornithine. comparison of two inactivators of ornithine aminotransferase[j]. biochemical journal, 1990, 268(2): 409-414.[2] rosenthal g a, rhodes d. l-canavanine transport and utilization in developing jack bean, canavalia ensiformis (l.) dc.[leguminosae][j]. plant physiology, 1984, 76(2): 541-544.[3] peraino c, bunville l g, tahmisian t n. chemical, physical, and morphological properties of ornithine aminotransferase from rat liver[j]. journal of biological chemistry, 1969, 244(9): 2241-2249.[4] rahiala e l, kekomki m, jnne j, et al. inhibition of pyridoxal enzymes by l-canaline[j]. biochimica et biophysica acta (bba)-enzymology, 1971, 227(2): 337-343.
Check Digit Verification of cas no
The CAS Registry Mumber 496-93-5 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,9 and 6 respectively; the second part has 2 digits, 9 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 496-93:
(5*4)+(4*9)+(3*6)+(2*9)+(1*3)=95
95 % 10 = 5
So 496-93-5 is a valid CAS Registry Number.
InChI:InChI=1/C4H10N2O3/c5-3(4(7)8)1-2-9-6/h3H,1-2,5-6H2,(H,7,8)
496-93-5Relevant articles and documents
Structure-activity studies of L-canaline-mediated inhibition of porcine alanine aminotransferase
Worthen, David R.,Ratliff, Darian K.,Rosenthal, Gerald A.,Trifonov,Crooks, Peter A.
, p. 1293 - 1297 (1996)
L-Canaline [L-2-amino-4-(aminooxy)butanoic acid] (L-CAN) and a family of eleven structurally related analogs were synthesized and evaluated for their inhibitory effect on PLP-dependent alanine aminotransferase (AlaAT) (EC 2.6.1.2) obtained from porcine heart. These congeners were selected to determine the stereochemical, aliphatic chain length, and aminooxy substitutional effects on L-CAN-mediated inhibition of AlaAT activity. L-CAN was the most effective inhibitor of the tested compounds; 10-7 M L-CAN elicited a 55% reduction in AlaAT activity after a 5 min exposure. This deleterious effect results from the ability of L-CAN to react avidly with the PLP moiety of the enzyme to form a stable, L-CAN-PLP oxime. In contrast, the methyl and ethyl esters of L-CAN reduced AlaAT activity by only 8% and 6%, respectively. While all of the L-enantiomeric forms of the tested compound were more potent AlaAT inhibitors than their corresponding D-stereoisomers, the D-enantiomers, particularly D-canaline, were active. Chain shortening or lengthening dramatically curtailed L-CAN-mediated loss in AlaAT activity, but the replacement of the α-amino group with a hydrogen was of little consequence in this regard. AlaAT was treated with L-CAN in the presence of free PLP to assess PLP capacity to protect AlaAT against 10-7 M L-CAN- dependent inactivation. L-CAN retained approximately two-thirds of its inhibitory ability in the presence of equimolar PLP, but AlaAT inhibition was reduced 90% by a 10-fold excess of PLP over L-CAN.
Synthesis of L-canaline and γ-functional 2-aminobutyric acid derivatives
Ozinskas,Rosenthal
, p. 5047 - 5050 (2007/10/02)
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